A mechanism with severing near barbed ends and annealing explains structure and dynamics of dendritic actin networks.

A mechanism with severing near barbed ends and annealing explains structure and dynamics of dendritic actin networks.
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DOI:
10.7554/elife.69031
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发表时间:
2022-06-07
期刊:
影响因子:
7.7
通讯作者:
Vavylonis, Dimitrios
Vavylonis, Dimitrios
中科院分区:
生物学1区
文献类型:
--
作者:
Holz, Danielle;Hall, Aaron R.;Usukura, Eiji;Yamashiro, Sawako;Watanabe, Naoki;Vavylonis, Dimitrios

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Single molecule imaging has shown that part of actin disassembles within a few seconds after incorporation into the dendritic filament network in lamellipodia, suggestive of frequent destabilization near barbed ends. To investigate the mechanisms behind network remodeling, we created a stochastic model with polymerization, depolymerization, branching, capping, uncapping, severing, oligomer diffusion, annealing, and debranching. We find that filament severing, enhanced near barbed ends, can explain the single molecule actin lifetime distribution, if oligomer fragments reanneal to free ends with rate constants comparable to in vitro measurements. The same mechanism leads to actin networks consistent with measured filament, end, and branch concentrations. These networks undergo structural remodeling, leading to longer filaments away from the leading edge, at the +/-35° orientation pattern. Imaging of actin speckle lifetimes at sub-second resolution verifies frequent disassembly of newly-assembled actin. We thus propose a unified mechanism that fits a diverse set of basic lamellipodia phenomenology.
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